LHP1_ARATH
ID LHP1_ARATH Reviewed; 445 AA.
AC Q946J8; Q9FN82;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Chromo domain-containing protein LHP1 {ECO:0000305};
DE AltName: Full=Protein LIKE HETEROCHROMATIN PROTEIN 1 {ECO:0000303|PubMed:11731464};
DE AltName: Full=Protein TERMINAL FLOWER 2 {ECO:0000303|PubMed:12826620, ECO:0000303|PubMed:9611176};
GN Name=LHP1 {ECO:0000303|PubMed:11731464};
GN Synonyms=TFL2 {ECO:0000303|PubMed:12826620, ECO:0000303|PubMed:9611176},
GN TU8 {ECO:0000303|PubMed:15356387};
GN OrderedLocusNames=At5g17690 {ECO:0000312|Araport:AT5G17690};
GN ORFNames=MVA3.4 {ECO:0000312|EMBL:BAB09568.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, FUNCTION, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=11731464; DOI=10.1242/dev.128.23.4847;
RA Gaudin V., Libault M., Pouteau S., Juul T., Zhao G., Lefebvre D.,
RA Grandjean O.;
RT "Mutations in LIKE HETEROCHROMATIN PROTEIN 1 affect flowering time and
RT plant architecture in Arabidopsis.";
RL Development 128:4847-4858(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12826620; DOI=10.1093/pcp/pcg091;
RA Kotake T., Takada S., Nakahigashi K., Ohto M., Goto K.;
RT "Arabidopsis TERMINAL FLOWER 2 gene encodes a heterochromatin protein 1
RT homolog and represses both FLOWERING LOCUS T to regulate flowering time and
RT several floral homeotic genes.";
RL Plant Cell Physiol. 44:555-564(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=9611176; DOI=10.1093/genetics/149.2.597;
RA Larsson A.S., Landberg K., Meeks-Wagner D.R.;
RT "The TERMINAL FLOWER2 (TFL2) gene controls the reproductive transition and
RT meristem identity in Arabidopsis thaliana.";
RL Genetics 149:597-605(1998).
RN [6]
RP INTERACTION WITH H3 AND CMT3.
RX PubMed=11898023; DOI=10.1038/nature731;
RA Jackson J.P., Lindroth A.M., Cao X., Jacobsen S.E.;
RT "Control of CpNpG DNA methylation by the KRYPTONITE histone H3
RT methyltransferase.";
RL Nature 416:556-560(2002).
RN [7]
RP INTERACTION WITH SUVH.
RX PubMed=15546353; DOI=10.1111/j.1365-313x.2004.02240.x;
RA Yu Y., Dong A., Shen W.-H.;
RT "Molecular characterization of the tobacco SET domain protein NtSET1
RT unravels its role in histone methylation, chromatin binding, and
RT segregation.";
RL Plant J. 40:699-711(2004).
RN [8]
RP FUNCTION.
RX PubMed=15356387; DOI=10.1023/b:plan.0000040897.49151.98;
RA Kim J.H., Durrett T.P., Last R.L., Jander G.;
RT "Characterization of the Arabidopsis TU8 glucosinolate mutation, an allele
RT of TERMINAL FLOWER2.";
RL Plant Mol. Biol. 54:671-682(2004).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=16244868; DOI=10.1007/s00425-005-0129-4;
RA Libault M., Tessadori F., Germann S., Snijder B., Fransz P., Gaudin V.;
RT "The Arabidopsis LHP1 protein is a component of euchromatin.";
RL Planta 222:910-925(2005).
RN [10]
RP FUNCTION.
RX PubMed=16549797; DOI=10.1073/pnas.0507427103;
RA Mylne J.S., Barrett L., Tessadori F., Mesnage S., Johnson L.,
RA Bernatavichute Y.V., Jacobsen S.E., Fransz P., Dean C.;
RT "LHP1, the Arabidopsis homologue of HETEROCHROMATIN PROTEIN1, is required
RT for epigenetic silencing of FLC.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5012-5017(2006).
RN [11]
RP FUNCTION.
RX PubMed=16682972; DOI=10.1038/ng1795;
RA Sung S., He Y., Eshoo T.W., Tamada Y., Johnson L., Nakahigashi K., Goto K.,
RA Jacobsen S.E., Amasino R.M.;
RT "Epigenetic maintenance of the vernalized state in Arabidopsis thaliana
RT requires LIKE HETEROCHROMATIN PROTEIN 1.";
RL Nat. Genet. 38:706-710(2006).
RN [12]
RP MUTAGENESIS OF TRP-132, AND SUBCELLULAR LOCATION.
RX PubMed=16361394; DOI=10.1105/tpc.105.036855;
RA Zemach A., Li Y., Ben-Meir H., Oliva M., Mosquna A., Kiss V., Avivi Y.,
RA Ohad N., Grafi G.;
RT "Different domains control the localization and mobility of LIKE
RT HETEROCHROMATIN PROTEIN1 in Arabidopsis nuclei.";
RL Plant Cell 18:133-145(2006).
RN [13]
RP FUNCTION, INTERACTION WITH RING1A, AND COMPONENT OF THE PRC1-LIKE COMPLEX.
RX PubMed=19097900; DOI=10.1016/j.cub.2008.11.019;
RA Xu L., Shen W.H.;
RT "Polycomb silencing of KNOX genes confines shoot stem cell niches in
RT Arabidopsis.";
RL Curr. Biol. 18:1966-1971(2008).
RN [14]
RP INTERACTION WITH POL2A.
RX PubMed=19947980; DOI=10.1111/j.1365-313x.2009.04093.x;
RA del Olmo I., Lopez-Gonzalez L., Martin-Trillo M.M., Martinez-Zapater J.M.,
RA Pineiro M., Jarillo J.A.;
RT "EARLY IN SHORT DAYS 7 (ESD7) encodes the catalytic subunit of DNA
RT polymerase epsilon and is required for flowering repression through a
RT mechanism involving epigenetic gene silencing.";
RL Plant J. 61:623-636(2010).
RN [15]
RP INTERACTION WITH CYP71.
RX PubMed=21596687; DOI=10.1093/mp/ssr036;
RA Li H., Luan S.;
RT "The cyclophilin AtCYP71 interacts with CAF-1 and LHP1 and functions in
RT multiple chromatin remodeling processes.";
RL Mol. Plant 4:748-758(2011).
RN [16]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH LIF2.
RC STRAIN=cv. Columbia;
RX PubMed=21304947; DOI=10.1371/journal.pone.0016592;
RA Latrasse D., Germann S., Houba-Herin N., Dubois E., Bui-Prodhomme D.,
RA Hourcade D., Juul-Jensen T., Le Roux C., Majira A., Simoncello N.,
RA Granier F., Taconnat L., Renou J.P., Gaudin V.;
RT "Control of flowering and cell fate by LIF2, an RNA binding partner of the
RT polycomb complex component LHP1.";
RL PLoS ONE 6:E16592-E16592(2011).
RN [17]
RP INTERACTION WITH DUF7/AIP1.
RX PubMed=26538092; DOI=10.1186/s12870-015-0641-z;
RA Brasil J.N., Cabral L.M., Eloy N.B., Primo L.M., Barroso-Neto I.L.,
RA Grangeiro L.P., Gonzalez N., Inze D., Ferreira P.C., Hemerly A.S.;
RT "AIP1 is a novel Agenet/Tudor domain protein from Arabidopsis that
RT interacts with regulators of DNA replication, transcription and chromatin
RT remodeling.";
RL BMC Plant Biol. 15:270-270(2015).
RN [18]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=27495811; DOI=10.1105/tpc.16.00244;
RA Molitor A., Latrasse D., Zytnicki M., Andrey P., Houba-Herin N., Hachet M.,
RA Battail C., Del Prete S., Alberti A., Quesneville H., Gaudin V.;
RT "The Arabidopsis hnRNP-Q Protein LIF2 and the PRC1 subunit LHP1 function in
RT concert to regulate the transcription of stress-responsive genes.";
RL Plant Cell 28:2197-2211(2016).
RN [19]
RP DISRUPTION PHENOTYPE, AND INTERACTION WITH EOL1.
RC STRAIN=cv. Columbia;
RX PubMed=28428341; DOI=10.1073/pnas.1620955114;
RA Zhou Y., Tergemina E., Cui H., Foerderer A., Hartwig B.,
RA Velikkakam James G., Schneeberger K., Turck F.;
RT "Ctf4-related protein recruits LHP1-PRC2 to maintain H3K27me3 levels in
RT dividing cells in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:4833-4838(2017).
RN [20]
RP INTERACTION WITH PDP3; MSI4/FVE AND MSI5, AND SUBUNIT.
RX PubMed=29314758; DOI=10.1111/jipb.12630;
RA Zhou J.X., Liu Z.W., Li Y.Q., Li L., Wang B., Chen S., He X.J.;
RT "Arabidopsis PWWP domain proteins mediate H3K27 trimethylation on FLC and
RT regulate flowering time.";
RL J. Integr. Plant Biol. 60:362-368(2018).
CC -!- FUNCTION: Structural component of heterochromatin involved in gene
CC repression, including several floral homeotic genes and FLT that
CC regulates flowering time (PubMed:9611176). Required for maintenance of
CC vernalization-induced repression of FLC. As part of the PRC1-like
CC complex, recognizes and binds histone H3 tails methylated at 'Lys-9'
CC (H3K9me) and 'Lys-27' (H3K27me), leading to epigenetic repression. PcG
CC PRC1 complex maintains the transcriptionally repressive state of many
CC genes, including Hox genes, throughout development. PcG PRC1 complex
CC acts via chromatin remodeling and modification of histones, rendering
CC chromatin heritably changed in its expressibility. Transcriptional
CC repressor that binds DNA on GAGA-like motif and 5'-(A/G/T)AACCCTA(A/G)-
CC 3' consensus motif in the promoters of target genes. Recognizes and
CC binds histone H3 tails methylated at 'Lys-27' (H3K27me) but depleted in
CC active histone marks such as H3K4me, leading to epigenetic repression.
CC When in complex with LHP1, recognizes and binds histone H3 tails
CC methylated at 'Lys-4' (H3K4me) and 'Lys-27' (H3K27me), mostly
CC corresponding to stress-responsive genes (PubMed:27495811).
CC {ECO:0000269|PubMed:11731464, ECO:0000269|PubMed:12826620,
CC ECO:0000269|PubMed:15356387, ECO:0000269|PubMed:16549797,
CC ECO:0000269|PubMed:16682972, ECO:0000269|PubMed:19097900,
CC ECO:0000269|PubMed:27495811, ECO:0000269|PubMed:9611176}.
CC -!- SUBUNIT: Homodimer (PubMed:11731464). Interacts with CYP71
CC (PubMed:21596687). Interacts with histone H3 and CMT3
CC (PubMed:11898023). Interacts with SUVH (PubMed:15546353). Component of
CC the PRC1-like complex, at least composed of RING1A, RING1B and LHP1
CC (PubMed:19097900). Binds to POL2A (PubMed:19097900). Interacts with
CC DUF7/AIP1 (PubMed:26538092). Binds to LIF2 in the nucleus on a common
CC set of chromatin regions (PubMed:21304947, PubMed:27495811). Interacts
CC with PDP3, MSI4/FVE and MSI5 (PubMed:29314758). Component of the PRC2
CC (polycomb repressive complex 2) complex which regulates histone
CC methylation on histone H3K27 (PubMed:29314758). Interacts with EOL1
CC (PubMed:28428341). {ECO:0000269|PubMed:11731464,
CC ECO:0000269|PubMed:11898023, ECO:0000269|PubMed:15546353,
CC ECO:0000269|PubMed:19097900, ECO:0000269|PubMed:21304947,
CC ECO:0000269|PubMed:21596687, ECO:0000269|PubMed:26538092,
CC ECO:0000269|PubMed:27495811, ECO:0000269|PubMed:28428341,
CC ECO:0000269|PubMed:29314758}.
CC -!- INTERACTION:
CC Q946J8; Q06850: CPK1; NbExp=3; IntAct=EBI-2309089, EBI-2357775;
CC Q946J8; Q8LAL2: IAA26; NbExp=3; IntAct=EBI-2309089, EBI-3947418;
CC Q946J8; Q946J8: LHP1; NbExp=3; IntAct=EBI-2309089, EBI-2309089;
CC Q946J8; O22467: MSI1; NbExp=4; IntAct=EBI-2309089, EBI-632891;
CC Q946J8; O23160: MYB73; NbExp=3; IntAct=EBI-2309089, EBI-25506855;
CC Q946J8; Q7XA73: TIFY4A; NbExp=5; IntAct=EBI-2309089, EBI-15199673;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11731464,
CC ECO:0000269|PubMed:12826620, ECO:0000269|PubMed:16244868,
CC ECO:0000269|PubMed:16361394, ECO:0000269|PubMed:21304947}.
CC Note=Punctuated distribution and in heterochromatic chromocenters.
CC -!- TISSUE SPECIFICITY: Mainly expressed in meristematic tissues of
CC vegetative, inflorescence and floral organs, like in developing ovules,
CC petals, root pericycle, petiole and petiole side of developing leaf
CC blade or vascular tissue. {ECO:0000269|PubMed:11731464,
CC ECO:0000269|PubMed:12826620}.
CC -!- DOMAIN: The chromo domain specifically binds to dimethylated H3 'Lys-9'
CC while the chromo shadow domain is required for dimerization.
CC -!- DISRUPTION PHENOTYPE: Dwarf plants with early flowering and
CC inflorescences termination with floral structures in both long days and
CC short days (PubMed:9611176). Phenotypes of the lhp1-3 mutant are
CC enhanced by the disruption of EOL1, thus leading to reduced plant size,
CC early flowering in all photoperiod conditions and altered leaf
CC morphology, associated with an increased expression of H3K27me3-
CC positive genes (PubMed:28428341). {ECO:0000269|PubMed:28428341,
CC ECO:0000269|PubMed:9611176}.
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DR EMBL; AF387639; AAL04059.1; -; mRNA.
DR EMBL; AB073490; BAB70689.1; -; Genomic_DNA.
DR EMBL; AB006706; BAB09568.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92456.1; -; Genomic_DNA.
DR RefSeq; NP_197271.1; NM_121775.3.
DR PDB; 7VYW; X-ray; 1.60 A; A=106-160.
DR PDB; 7VZ2; X-ray; 1.70 A; A=106-160.
DR PDBsum; 7VYW; -.
DR PDBsum; 7VZ2; -.
DR AlphaFoldDB; Q946J8; -.
DR SMR; Q946J8; -.
DR BioGRID; 16911; 26.
DR DIP; DIP-54865N; -.
DR IntAct; Q946J8; 8.
DR STRING; 3702.AT5G17690.1; -.
DR iPTMnet; Q946J8; -.
DR PaxDb; Q946J8; -.
DR PRIDE; Q946J8; -.
DR EnsemblPlants; AT5G17690.1; AT5G17690.1; AT5G17690.
DR GeneID; 831635; -.
DR Gramene; AT5G17690.1; AT5G17690.1; AT5G17690.
DR KEGG; ath:AT5G17690; -.
DR Araport; AT5G17690; -.
DR TAIR; locus:2176006; AT5G17690.
DR eggNOG; KOG1911; Eukaryota.
DR HOGENOM; CLU_035097_1_0_1; -.
DR InParanoid; Q946J8; -.
DR PhylomeDB; Q946J8; -.
DR PRO; PR:Q946J8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q946J8; baseline and differential.
DR Genevisible; Q946J8; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA:TAIR.
DR GO; GO:0000792; C:heterochromatin; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035064; F:methylated histone binding; IDA:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IMP:TAIR.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0031507; P:heterochromatin assembly; IEA:InterPro.
DR GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
DR GO; GO:0009910; P:negative regulation of flower development; IMP:TAIR.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IMP:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0009648; P:photoperiodism; IMP:TAIR.
DR GO; GO:0048573; P:photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0010016; P:shoot system morphogenesis; IMP:TAIR.
DR GO; GO:0010048; P:vernalization response; IMP:TAIR.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR017984; Chromo_dom_subgr.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR008251; Chromo_shadow_dom.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR044251; LHP1-like.
DR PANTHER; PTHR47240; PTHR47240; 1.
DR Pfam; PF00385; Chromo; 1.
DR PRINTS; PR00504; CHROMODOMAIN.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00300; ChSh; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Developmental protein; Differentiation;
KW Flowering; Nucleus; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..445
FT /note="Chromo domain-containing protein LHP1"
FT /id="PRO_0000247864"
FT DOMAIN 108..167
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 378..442
FT /note="Chromo 2; shadow subtype"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..178
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 22
FT /note="E -> D (in strain: cv. Landsberg erecta)"
FT MUTAGEN 132
FT /note="W->G: Loss of interaction with 'K-9' of H3 and loss
FT of chromocenter localization and punctuated distribution
FT inside the nucleus."
FT /evidence="ECO:0000269|PubMed:16361394"
SQ SEQUENCE 445 AA; 48644 MW; FE68BD510376D622 CRC64;
MKGASGAVKK KPQVLNEAGE AETAVETVGE SRKISGDGGF GSDDGGGGGG GGSGESILRE
IGDDRPTEDG DEEEEEDEDE DDGGDEEDEE GEGEGGQEER PKLDEGFYEI EAIRRKRVRK
GKVQYLIKWR GWPETANTWE PLENLQSIAD VIDAFEGSLK PGKPGRKRKR KYAGPHSQMK
KKQRLTSTSH DATEKSDSST SLNNSSLPDI PDPLDLSGSS LLNRDVEAKN AYVSNQVEAN
SGSVGMARQV RLIDNEKEYD PTLNELRGPV NNSNGAGCSQ GGGIGSEGDN VRPNGLLKVY
PKELDKNSRF IGAKRRKSGS VKRFKQDGST SNNHTAPTDQ NLTPDLTTLD SFGRIARMGN
EYPGVMENCN LSQKTKIEEL DITKILKPMS FTASVSDNVQ EVLVTFLALR SDGKEALVDN
RFLKAHNPHL LIEFYEQHLK YNRTP
